Osteoarthritis (“OA”) is a degenerative joint disease characterized by cartilage damage and synovial inflammation. Previous data refer to changes to a molecular inflammatory cascade that lead to a destruction of cartilage macromolecules and irreversible morphological changes.1 Considerable evidence has shown that IL-1, Tumor Necrosis Factor-alpha, IL-6,8 and metalloproteinases are predominant catabolic and pro-inflammatory molecules playing a major role in pathogenesis of osteoarthritis.1 These cytokines are produced by activated synoviocytes, mononuclear cells or by articular cartilage itself, and their catabolic effect can be successfully blocked by inhibitory cytokines such as IL-4,10,13 and IL-1ra.1 
Similar inflammatory and catabolic pathways are involved in the pathogenesis of chronic tendonitis2 and chronic muscle tear healing failure.3 Tendon cells are subjected to continuous damage by producing increased levels of IL-1,6, metalloproteinases (MMPs) and other catabolic molecules.2 Pro-inflammatory cytokines IL-1 and TNF-alpha are involved in pathogenesis of chronic myositis3 as well. Atopic dermatitis (eczema) is considered as the most common relapsing inflammatory skin conditions. Chronic wound (including diabetic wound) is a wound that does not heal within three months due to poor circulation, neuropathy, immune disorders and complications of systemic illnesses, age, and repeated trauma. All mentioned conditions are characterized by disturbing cell signaling via cytokines and lost extracellular matrix (ECM) that forms the largest component of the dermal skin layer. Targeting special inflammatory and catabolic molecular pathways can have a beneficial therapeutic effect for inflammatory pathologies. This effect could be achieved by using therapeutically active proteins. Presently, the pharmaceutical industry employs high-cost molecular genetic technologies for recombinant protein production such as insulin, interferons, blood clotting factors, etc. However, these methods of recombinant protein generation include the expression of human genes in a bacterial cell. The patterns of post-translation protein modification including glycosylation may be different than those naturally occurring in humans. This may result in instability of the product in the human environment, decreasing of biological function or immune response provocation. Additionally, the cost of the final recombinant product is extremely high.